Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
3R01GM033851-08S1
Application #
3283971
Study Section
Physical Biochemistry Study Section (PB)
Project Start
1984-09-27
Project End
1993-08-31
Budget Start
1992-09-01
Budget End
1993-08-31
Support Year
8
Fiscal Year
1993
Total Cost
Indirect Cost
Name
Washington University
Department
Type
Schools of Medicine
DUNS #
062761671
City
Saint Louis
State
MO
Country
United States
Zip Code
63130
Kurz, Linda C; Constantine, Charles Z; Jiang, Hong et al. (2009) The partial substrate dethiaacetyl-coenzyme A mimics all critical carbon acid reactions in the condensation half-reaction catalyzed by Thermoplasma acidophilum citrate synthase. Biochemistry 48:7878-91
Kurz, Linda C; Fite, Brett; Jean, John et al. (2005) Photophysics of tryptophan fluorescence: link with the catalytic strategy of the citrate synthase from Thermoplasma acidophilum. Biochemistry 44:1394-413
Deng, Hua; Cahill, Sean; Kurz, Linda et al. (2004) The assignment of downfield proton resonances in an enzyme inhibitor complex using time-dependent saturation transferred NOEs. J Am Chem Soc 126:1952-3
Kurz, L C; Drysdale, G; Riley, M et al. (2000) Kinetics and mechanism of the citrate synthase from the thermophilic archaeon Thermoplasma acidophilum. Biochemistry 39:2283-96
Gu, Z; Drueckhammer, D G; Kurz, L et al. (1999) Solid state NMR studies of hydrogen bonding in a citrate synthase inhibitor complex. Biochemistry 38:8022-31
Kurz, L C; Nakra, T; Stein, R et al. (1998) Effects of changes in three catalytic residues on the relative stabilities of some of the intermediates and transition states in the citrate synthase reaction. Biochemistry 37:9724-37
Deng, H; Kurz, L C; Rudolph, F B et al. (1998) Characterization of hydrogen bonding in the complex of adenosine deaminase with a transition state analogue: a Raman spectroscopic study. Biochemistry 37:4968-76
Kurz, L C; Roble, J H; Nakra, T et al. (1997) Ability of single-site mutants of citrate synthase to catalyze proton transfer from the methyl group of dethiaacetyl-coenzyme A, a non-thioester substrate analog. Biochemistry 36:3981-90
Evans, C T; Kurz, L C; Remington, S J et al. (1996) Active site mutants of pig citrate synthase: effects of mutations on the enzyme catalytic and structural properties. Biochemistry 35:10661-72
Sideraki, V; Wilson, D K; Kurz, L C et al. (1996) Site-directed mutagenesis of histidine 238 in mouse adenosine deaminase: substitution of histidine 238 does not impede hydroxylate formation. Biochemistry 35:15019-28

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